recommended for detection of Ser 21 phosphorylated GSK-3β of human origin by WB, IP and ELISA
Modification
Phosphoralated
Modification Notes
Glycogen synthase kinase-3å (GSK-3å) and GSK-3∫ are highly similar isoforms of serine/ threonine kinases that regulate metabolic enzymes and transcription factors, which are responsible for coordinating processes such as glycogen synthesis and cell adhesion. GSK-3∫ activity is also required for nuclear activity of Rel dimers, which mediate an anti-apoptotic response to TNFå in mice. GSK-3 catalytic kinase activity is controlled through differential phosphorylation of serine/threonine residues, which have an inhibitory effect, and tyrosine residues, which have an activating effect. Growth factor stimulation of mammalian cells expressing GSK-3å and GSK-3∫ induces phosphorylation of Ser 21 and Ser 9, respectively, through a phosphatidylinositol 3-kinase (PI 3-K)-protein kinase B (PKB)-dependent pathway, thereby enhancing proliferative signals. Additionally, GSK-3 physically associates with cAMP-dependent protein kinase A (PKA), which phosphorylates Ser 21 of GSK-3å or Ser 9 of GSK-3∫ and inactivates both forms. GSK-3å/∫ is positively regulated by phosphorylation on Tyr 279 and Tyr 216, respectively. Activated GSK-3å/∫ participates in energy metabolism, neuronal cell development, and body pattern formation. Tyrosine dephosphorylation of GSK-3 is involved in its extracellular signal-dependent inactivation.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPELISA
WB:1:500~1:2000 IP:1:100~1:500 Notes:Optimal dilutions/concentrations should be determined by the researcher.
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
recommended for detection of Ser 21 phosphorylated GSK-3&beta of human origin by WB IP and ELISA
Tissue Specificity
recommended for detection of Ser 21 phosphorylated GSK-3β of human origin by WB, IP and ELISA